3Q11
Crystals Structure of Aspartate beta-Semialdehyde Dehydrogenase from Streptococcus pneumoniae with NADP and aspartyl beta-difluorophosphonate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004073 | molecular_function | aspartate-semialdehyde dehydrogenase activity |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0009086 | biological_process | methionine biosynthetic process |
A | 0009088 | biological_process | threonine biosynthetic process |
A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
A | 0009097 | biological_process | isoleucine biosynthetic process |
A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
A | 0046983 | molecular_function | protein dimerization activity |
A | 0050661 | molecular_function | NADP binding |
A | 0051287 | molecular_function | NAD binding |
B | 0004073 | molecular_function | aspartate-semialdehyde dehydrogenase activity |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0009086 | biological_process | methionine biosynthetic process |
B | 0009088 | biological_process | threonine biosynthetic process |
B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
B | 0009097 | biological_process | isoleucine biosynthetic process |
B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
B | 0046983 | molecular_function | protein dimerization activity |
B | 0050661 | molecular_function | NADP binding |
B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE NAP A 367 |
Chain | Residue |
A | GLY9 |
A | ALA72 |
A | THR76 |
A | GLY161 |
A | MET162 |
A | GLY163 |
A | HOH644 |
A | HOH653 |
A | HOH727 |
A | HOH816 |
A | THR11 |
A | GLY12 |
A | ALA13 |
A | ALA36 |
A | SER37 |
A | ARG39 |
A | SER40 |
A | THR57 |
site_id | AC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE NAP B 367 |
Chain | Residue |
B | GLY9 |
B | THR11 |
B | GLY12 |
B | ALA13 |
B | ALA36 |
B | SER37 |
B | ARG39 |
B | SER40 |
B | ALA72 |
B | THR76 |
B | ALA160 |
B | GLY161 |
B | MET162 |
B | GLY163 |
B | LEU166 |
B | HOH447 |
B | HOH631 |
B | HOH649 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE P4F A 368 |
Chain | Residue |
A | ASN94 |
A | ARG99 |
A | ASN127 |
A | CYS128 |
A | GLN155 |
A | GLY159 |
A | ILE209 |
A | GLU220 |
A | LYS223 |
A | ARG245 |
A | HIS252 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE P4F B 368 |
Chain | Residue |
B | ARG99 |
B | ASN127 |
B | CYS128 |
B | GLN155 |
B | GLY159 |
B | ILE209 |
B | GLU220 |
B | LYS223 |
B | ARG245 |
B | HIS252 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 369 |
Chain | Residue |
A | GLU343 |
B | ALA274 |
B | PHE276 |
B | ALA279 |
B | HOH698 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO B 369 |
Chain | Residue |
A | THR26 |
A | EDO370 |
B | GLU24 |
B | SER25 |
B | TRP332 |
B | GLU339 |
B | HOH387 |
B | HOH446 |
B | HOH526 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO A 370 |
Chain | Residue |
A | GLU24 |
A | SER25 |
A | TRP332 |
A | GLU339 |
A | HOH439 |
A | HOH481 |
B | THR26 |
B | EDO369 |
B | HOH526 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 371 |
Chain | Residue |
A | SER250 |
A | GLY298 |
A | ASP324 |
A | LEU326 |
A | HOH377 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 370 |
Chain | Residue |
B | SER250 |
B | GLY298 |
B | ASP324 |
B | LEU326 |
B | HOH532 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 372 |
Chain | Residue |
A | LEU311 |
A | ASP312 |
A | HOH415 |
B | LYS229 |